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Literature summary for 3.1.3.16 extracted from

  • Klee, C.B.; Krinks, M.H.; Manalan, A.S.; Draetta, G.F.; Newton, D.L.
    Control of calcineurin protein phosphatase activity (1985), Adv. Protein Phosphatases, 1, 135-146.
No PubMed abstract available

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+
-
Mammalia
Co2+
-
Oryctolagus cuniculus
Mg2+
-
Mammalia
Mg2+
-
Oryctolagus cuniculus
Ni2+ activation Mammalia
Ni2+ activation Oryctolagus cuniculus
Zn2+
-
Mammalia

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000 90000 phosphatase 2B, i.e. calcineurin, sedimentation equilibrium centrifugation Mammalia
80000 90000 phosphatase 2B, i.e. calcineurin, sedimentation equilibrium centrifugation Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Mammalia
-
-
-
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Mammalia
-
brain
-
Oryctolagus cuniculus
-
additional information
-
Mammalia
-
additional information
-
Oryctolagus cuniculus
-
skeletal muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoproteins + H2O
-
Oryctolagus cuniculus proteins + phosphate
-
?
phosphoproteins + H2O most of the substrates are phosphorylated by cAMP and cGMP dependent protein kinases, other substrates are phosphorylated by calmodulin dependent multiprotein kinase Mammalia proteins + phosphate
-
?

Subunits

Subunits Comment Organism
dimer
-
Mammalia

Cofactor

Cofactor Comment Organism Structure
Calmodulin activation, dependent on Ca2+ Mammalia
Calmodulin activation, dependent on Ca2+ Oryctolagus cuniculus